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New page: left|200px<br /> <applet load="1gsd" size="450" color="white" frame="true" align="right" spinBox="true" caption="1gsd, resolution 2.5Å" /> '''GLUTATHIONE TRANSFER...
 
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[[Image:1gsd.gif|left|200px]]<br />
<applet load="1gsd" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1gsd, resolution 2.5&Aring;" />
'''GLUTATHIONE TRANSFERASE A1-1 IN UNLIGANDED FORM'''<br />


==Overview==
==GLUTATHIONE TRANSFERASE A1-1 IN UNLIGANDED FORM==
BACKGROUND: Glutathione transferases (GSTs) constitute a family of, isoenzymes that catalyze the conjugation of the tripeptide glutathione, with a wide variety of hydrophobic compounds bearing an electrophilic, functional group. Recently, a number of X-ray structures have been, reported which have defined both the glutathione- and the, substrate-binding sites in these enzymes. The structure of the, glutathione-free enzyme from a mammalian source has not, however, been, reported previously. RESULTS: We have solved structures of a human, alpha-class GST, isoenzyme A1-1, both in the unliganded form and in, complexes with the inhibitor ethacrynic acid and its glutathione, conjugate. These structures have been refined to resolutions of 2.5 A, 2.7, A and 2.0 A respectively. Both forms of the inhibitor are clearly present, in the associated electron density. CONCLUSIONS: The major differences, among the three structures reported here involve the C-terminal, alpha-helix, which is a characteristic of the alpha-class enzyme. This, helix forms a lid over the active site when the hydrophobic substrate, binding site (H-site) is occupied but it is otherwise disordered., Ethacrynic acid appears to bind in a non-productive mode in the absence of, the coenzyme glutathione.
<StructureSection load='1gsd' size='340' side='right'caption='[[1gsd]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1gsd]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GSD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GSD FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5&#8491;</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1gsd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gsd OCA], [https://pdbe.org/1gsd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1gsd RCSB], [https://www.ebi.ac.uk/pdbsum/1gsd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1gsd ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/GSTA1_HUMAN GSTA1_HUMAN] Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles.<ref>PMID:20606271</ref>
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/gs/1gsd_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1gsd ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1GSD is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Active as [http://en.wikipedia.org/wiki/Glutathione_transferase Glutathione transferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.18 2.5.1.18] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1GSD OCA].
*[[Glutathione S-transferase 3D structures|Glutathione S-transferase 3D structures]]
 
== References ==
==Reference==
<references/>
Structural analysis of human alpha-class glutathione transferase A1-1 in the apo-form and in complexes with ethacrynic acid and its glutathione conjugate., Cameron AD, Sinning I, L'Hermite G, Olin B, Board PG, Mannervik B, Jones TA, Structure. 1995 Jul 15;3(7):717-27. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8591048 8591048]
__TOC__
[[Category: Glutathione transferase]]
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Cameron, A.D.]]
[[Category: Cameron AD]]
[[Category: Hermite, G.L.]]
[[Category: Jones TA]]
[[Category: Jones, T.A.]]
[[Category: L'Hermite G]]
[[Category: Sinning, I.]]
[[Category: Sinning I]]
[[Category: transferase (glutathione)]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 17:08:38 2007''

Latest revision as of 07:26, 7 February 2024

GLUTATHIONE TRANSFERASE A1-1 IN UNLIGANDED FORM

1gsd, resolution 2.50Å

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